To see the other types of publications on this topic, follow the link: Glycosylation.

Journal articles on the topic 'Glycosylation'

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Glycosylation.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Mendez-Yañez, Angela, Patricio Ramos, and Luis Morales-Quintana. "Role of Glycoproteins during Fruit Ripening and Seed Development." Cells 10, no. 8 (August 15, 2021): 2095. http://dx.doi.org/10.3390/cells10082095.

Full text
Abstract:
Approximately thirty percent of the proteins synthesized in animal or plant cells travel through the secretory pathway. Seventy to eighty percent of those proteins are glycosylated. Thus, glycosylation is an important protein modification that is related to many cellular processes, such as differentiation, recognition, development, signal transduction, and immune response. Additionally, glycosylation affects protein folding, solubility, stability, biogenesis, and activity. Specifically, in plants, glycosylation has recently been related to the fruit ripening process. This review aims to provide valuable information and discuss the available literature focused on three principal topics: (I) glycosylations as a key posttranslational modification in development in plants, (II) experimental and bioinformatics tools to analyze glycosylations, and (III) a literature review related to glycosylations in fruit ripening. Based on these three topics, we propose that it is necessary to increase the number of studies related to posttranslational modifications, specifically protein glycosylation because the specific role of glycosylation in the posttranslational process and how this process affects normal fruit development and ripening remain unclear to date.
APA, Harvard, Vancouver, ISO, and other styles
2

Mal, Dipakranjan, and Soumen Chakraborty. "C-Glycosylation of Substituted β-Naphthols with Trichloroacet­imidate Glycosyl Donors." Synthesis 50, no. 07 (January 3, 2018): 1560–68. http://dx.doi.org/10.1055/s-0036-1591746.

Full text
Abstract:
Several glycosyl donors have been systematically investigated for C-glycosylation of substituted β-naphthols to delineate the effect of the substituents. Whereas glycosylations of the parent 2-naphthol are smoothly achievable, those of differently substituted 2-naphthols are cumbersome. Efficiency of the glycosylation depends on the nature of both the glycosyl donors and the substituents of the arene ring. Among various glycosyl donors, trichloroacetimidate glycosyl donors are found to be superior for glycosylation with substituted 2-naphthols.
APA, Harvard, Vancouver, ISO, and other styles
3

Demeter, Fruzsina, Tímea Balogh, Tse-Kai Fu, Margaret Dah-Tsyr Chang, Yuan-Chuan Lee, Anikó Borbás, and Mihály Herczeg. "Preparation of α-l-Rhamnobiosides by Open and Conventional Glycosylations for Studies of the rHPL Lectin." Synlett 30, no. 19 (October 10, 2019): 2185–92. http://dx.doi.org/10.1055/s-0039-1690710.

Full text
Abstract:
To study the effect of oligosaccharides on biological systems (e.g., carbohydrate–lectin interactions), chemical synthesis of the desired carbohydrate derivatives is highly desirable, but it is usually a very complicated task. Most of the stereo- and regioselective glycosylation reactions are carried out by using protected acceptors and donors. At the same time, open glycosylation (use of an unprotected acceptor) may shorten the reaction pathway, if sufficient selectivity can be achieved between the acceptor hydroxyl groups. Toward synthesis of higher oligomers and multivalent derivatives, which are often useful for lectin binding studies, open glycosylation reactions of propargyl and phenylthio rhamnosides were investigated as a rapid route to the α-(1,3)-linked rhamnobioside binding motif. The efficacy of open glycosylations proved to be highly dependent on both the type of donor and the solvent applied. Using a trichloroacetimidate donor in 1,4-dioxane, the open glycosylation reactions proceeded with high regioselectivity and in good yields. Conventional glycosylations, on the other hand, afforded the α-(1,2)- and α-(1,3)-linked rhamnobioside derivatives with slightly higher yields via three-step longer syntheses.
APA, Harvard, Vancouver, ISO, and other styles
4

Pasing, Yvonne, Albert Sickmann, and Urs Lewandrowski. "N-glycoproteomics: mass spectrometry-based glycosylation site annotation." Biological Chemistry 393, no. 4 (April 1, 2012): 249–58. http://dx.doi.org/10.1515/hsz-2011-0245.

Full text
Abstract:
Abstract Glycosylations are ubiquitous and, in many cases, essential protein modifications. Yet comprehensive and detailed analysis of glycosylations on a proteome-wide scale is a daunting and still unsolved challenge. However, a common workflow has emerged over the last decade for large-scale N-glycosylation site annotation by application of proteomic methodology. Thereby, the qualitative and quantitative assessment of hundreds or thousands of modification sites is enabled. This review presents a short overview about common enrichment techniques and glycosylation site detection for N-glycopeptides, including benefits and challenges of analysis.
APA, Harvard, Vancouver, ISO, and other styles
5

Pal, Rita, Anupama Das, and Narayanaswamy Jayaraman. "One-pot oligosaccharide synthesis: latent-active method of glycosylations and radical halogenation activation of allyl glycosides." Pure and Applied Chemistry 91, no. 9 (September 25, 2019): 1451–70. http://dx.doi.org/10.1515/pac-2019-0306.

Full text
Abstract:
Abstract Chemical glycosylations occupy a central importance to synthesize tailor-made oligo- and polysaccharides of functional importance. Generation of the oxocarbenium ion or the glycosyl cation is the method of choice in order to form the glycosidic bond interconnecting a glycosyl moiety with a glycosyl/aglycosyl moiety. A number of elegant methods have been devised that allow the glycosyl cation formation in a fairly stream-lined manner to a large extent. The latent-active method provides a powerful approach in the protecting group controlled glycosylations. In this context, allyl glycosides have been developed to meet the requirement of latent-active reactivities under appropriate glycosylation conditions. Radical halogenation provides a newer route of activation of allyl glycosides to an activated allylic glycoside. Such an allylic halide activation subjects the glycoside reactive under acid catalysis, leading to the conversion to a glycosyl cation and subsequent glycosylation with a number of acceptors. The complete anomeric selectivity favoring the 1,2-trans-anomeric glycosides points to the possibility of a preferred conformation of the glycosyl cation. This article discusses about advancements in the selectivity of glycosylations, followed by delineating the allylic halogenation of allyl glycoside as a glycosylation method and demonstrates synthesis of a repertoire of di- and trisaccharides, including xylosides, with varied protecting groups.
APA, Harvard, Vancouver, ISO, and other styles
6

Brimble, Margaret A., Roger M. Davey, Malcolm D. McLeod, and Maureen Murphy. "C-Glycosylation of Oxygenated Naphthols with 3-Dimethylamino-2,3,6-trideoxy-L-arabino-hexopyranose and 3-Azido-2,3,6-trideoxy-D-arabino-hexopyranose." Australian Journal of Chemistry 56, no. 8 (2003): 787. http://dx.doi.org/10.1071/ch02236.

Full text
Abstract:
In connection with studies directed towards the synthesis of the pyranonaphthoquinone antibiotic medermycin, C-aryl glycosides were prepared by C-glycosylation of naphthols with glycosyl donors. Boron trifluoride diethyl etherate proved to be a suitable Lewis acid to promote the C-glycosylation, and use of the azido glycosyl donor proved more successful than using the dimethylamino glycosyl donor. 5-Hydroxy-1,4-dimethoxynaphthalene underwent facile C-glycosylation with two particular glycosyl donors, whereas 3-bromo-5-hydroxy-1,4-dimethoxynaphthalene was not an effective coupling partner with the same glycosyl donors. These studies indicate that subtle steric and electronic effects need to be considered in order to fine-tune C-glycosylations when using highly functionalized glycosyl donors.
APA, Harvard, Vancouver, ISO, and other styles
7

Mukherjee, Mana Mohan, Nabamita Basu, and Rina Ghosh. "Iron(iii) chloride modulated selective 1,2-trans glycosylation based on glycosyl trichloroacetimidate donors and its application in orthogonal glycosylation." RSC Advances 6, no. 107 (2016): 105589–606. http://dx.doi.org/10.1039/c6ra21859h.

Full text
Abstract:
FeCl3 modulated excellent 1,2-trans selective glycosylations based on trichloroacetimidate glycosyl donors even in the presence of apparently silent C-2 protecting group, along with orthogonal glycosylation reactions are reported.
APA, Harvard, Vancouver, ISO, and other styles
8

Deng, Li-Fan, Yingwei Wang, Shiyang Xu, Ao Shen, Hangping Zhu, Siyu Zhang, Xia Zhang, and Dawen Niu. "Palladium catalysis enables cross-coupling–like S N 2-glycosylation of phenols." Science 382, no. 6673 (November 24, 2023): 928–35. http://dx.doi.org/10.1126/science.adk1111.

Full text
Abstract:
Despite their importance in life and material sciences, the efficient construction of stereo-defined glycosides remains a challenge. Studies of carbohydrate functions would be advanced if glycosylation methods were as reliable and modular as palladium (Pd)-catalyzed cross-coupling. However, Pd-catalysis excels in forming sp 2 -hybridized carbon centers whereas glycosylation mostly builds sp 3 -hybridized C–O linkages. We report a glycosylation platform through Pd-catalyzed S N 2 displacement from phenols toward bench-stable, aryl-iodide–containing glycosyl sulfides. The key Pd(II) oxidative addition intermediate diverges from an arylating agent (Csp 2 electrophile) to a glycosylating agent (Csp 3 electrophile). This method inherits many merits of cross-coupling reactions, including operational simplicity and functional group tolerance. It preserves the S N 2 mechanism for various substrates and is amenable to late-stage glycosylation of commercial drugs and natural products.
APA, Harvard, Vancouver, ISO, and other styles
9

Yang, Weizhun, Bo Yang, Sherif Ramadan, and Xuefei Huang. "Preactivation-based chemoselective glycosylations: A powerful strategy for oligosaccharide assembly." Beilstein Journal of Organic Chemistry 13 (October 9, 2017): 2094–114. http://dx.doi.org/10.3762/bjoc.13.207.

Full text
Abstract:
Most glycosylation reactions are performed by mixing the glycosyl donor and acceptor together followed by the addition of a promoter. While many oligosaccharides have been synthesized successfully using this premixed strategy, extensive protective group manipulation and aglycon adjustment often need to be performed on oligosaccharide intermediates, which lower the overall synthetic efficiency. Preactivation-based glycosylation refers to strategies where the glycosyl donor is activated by a promoter in the absence of an acceptor. The subsequent acceptor addition then leads to the formation of the glycoside product. As donor activation and glycosylation are carried out in two distinct steps, unique chemoselectivities can be obtained. Successful glycosylation can be performed independent of anomeric reactivities of the building blocks. In addition, one-pot protocols have been developed that have enabled multiple-step glycosylations in the same reaction flask without the need for intermediate purification. Complex glycans containing both 1,2-cis and 1,2-trans linkages, branched oligosaccharides, uronic acids, sialic acids, modifications such as sulfate esters and deoxy glycosides have been successfully synthesized. The preactivation-based chemoselective glycosylation is a powerful strategy for oligosaccharide assembly complementing the more traditional premixed method.
APA, Harvard, Vancouver, ISO, and other styles
10

Mestrom, Przypis, Kowalczykiewicz, Pollender, Kumpf, Marsden, Bento, et al. "Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach." International Journal of Molecular Sciences 20, no. 21 (October 23, 2019): 5263. http://dx.doi.org/10.3390/ijms20215263.

Full text
Abstract:
Enzymes are nature’s catalyst of choice for the highly selective and efficient coupling of carbohydrates. Enzymatic sugar coupling is a competitive technology for industrial glycosylation reactions, since chemical synthetic routes require extensive use of laborious protection group manipulations and often lack regio- and stereoselectivity. The application of Leloir glycosyltransferases has received considerable attention in recent years and offers excellent control over the reactivity and selectivity of glycosylation reactions with unprotected carbohydrates, paving the way for previously inaccessible synthetic routes. The development of nucleotide recycling cascades has allowed for the efficient production and reuse of nucleotide sugar donors in robust one-pot multi-enzyme glycosylation cascades. In this way, large glycans and glycoconjugates with complex stereochemistry can be constructed. With recent advances, LeLoir glycosyltransferases are close to being applied industrially in multi-enzyme, programmable cascade glycosylations.
APA, Harvard, Vancouver, ISO, and other styles
11

Wu, Jun, Nikolaos Kaplaneris, Shaofei Ni, Felix Kaltenhäuser, and Lutz Ackermann. "Late-stage C(sp2)–H and C(sp3)–H glycosylation of C-aryl/alkyl glycopeptides: mechanistic insights and fluorescence labeling." Chemical Science 11, no. 25 (2020): 6521–26. http://dx.doi.org/10.1039/d0sc01260b.

Full text
Abstract:
C–H glycosylations of complex amino acids and peptides were accomplished through the assistance of triazole peptide-isosteres. The palladium-catalyzed glycosylation provided access to complex C-glycosides and fluorescent-labeled glycoamino acids.
APA, Harvard, Vancouver, ISO, and other styles
12

Whitfield, Dennis M., Stephen P. Douglas, Ting-Hua Tang, Imre G. Csizmadia, Henrianna Y. S. Pang, Frederick L. Moolten, and Jiri J. Krepinsky. "Differential reactivity of carbohydrate hydroxyls in glycosylations. II. The likely role of intramolecular hydrogen bonding on glycosylation reactions. Galactosylation of nucleoside 5′-hydroxyls for the syntheses of novel potential anticancer agents." Canadian Journal of Chemistry 72, no. 11 (November 1, 1994): 2225–38. http://dx.doi.org/10.1139/v94-284.

Full text
Abstract:
Contrary to expectations, many primary hydroxy groups are completely unreactive in glycosylation reactions, or give the desired glycosides in very low yields accompanied by products of many side reactions. Hydrogens of such primary hydroxyls are shown to be intramolecularly hydrogen bonded. Intermediates formed by nucleophilic attack by these hydroxyls on activated glycosylating agents may resist hydrogen abstraction. This resistance to proton loss is postulated to be the origin of the observed unreactivity. It is shown that successful glycosylations take place under acidic conditions under which such hydrogen bonds cease to exist. Accordingly, direct galactosylations of the normally unreactive 5′-hydroxyls of nucleosides were accomplished for the first time with a galactose trichloroacetimidate donor in chloroform under silver triflate promotion. It is noted that such galactosylated anticancer nucleosides may have improved biological specificity.
APA, Harvard, Vancouver, ISO, and other styles
13

Hsu, Mei-Yuan, Sarah Lam, Chia-Hui Wu, Mei-Huei Lin, Su-Ching Lin, and Cheng-Chung Wang. "Direct Dehydrative Glycosylation Catalyzed by Diphenylammonium Triflate." Molecules 25, no. 5 (March 2, 2020): 1103. http://dx.doi.org/10.3390/molecules25051103.

Full text
Abstract:
Methods for direct dehydrative glycosylations of carbohydrate hemiacetals catalyzed by diphenylammonium triflate under microwave irradiation are described. Both armed and disarmed glycosyl-C1-hemiacetal donors were efficiently glycosylated in moderate to excellent yields without the need for any drying agents and stoichiometric additives. This method has been successfully applied to a solid-phase glycosylation.
APA, Harvard, Vancouver, ISO, and other styles
14

Jaeken, Jaak, and Gert Matthijs. "From glycosylation to glycosylation diseases." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1792, no. 9 (September 2009): 823. http://dx.doi.org/10.1016/j.bbadis.2009.08.003.

Full text
APA, Harvard, Vancouver, ISO, and other styles
15

Li, Chunbao, Wenjiao Yuan, and Yali Liu. "A Rapid and Diastereoselective Synthesis of 2-Deoxy-2-iodo-α-glycosides and its Mechanism for Diastereoselectivity." Synlett 28, no. 15 (May 24, 2017): 1975–78. http://dx.doi.org/10.1055/s-0036-1588440.

Full text
Abstract:
Reductive deiodination of 2-deoxy-2-iodo-glycoside is an efficient and practical approach for the synthesis of 2-deoxyglycosides, which are moieties of bioactive compounds. However, inseparable diastereoisomers are usually formed in the preparation of 2-deoxy-2-iodo-glycosides via glycosylation of glycals with alcohols using current methods. To overcome this problem, a rapid and diastereoselective transformation of glycals and alcohols into 2-deoxy-2-iodo-α-glycosides enabled by I2/PhI(OAc)2 has been developed. 14 glycals, derived from 13 monosaccharides and one disaccharide, diastereoselectively yielded α-glycosides. Only in two cases the diastereoselectivity of the glycosylation was poor. The yields of glycosylation range from 73% to 95%, and the reactions are finished in only five minutes. Investigations for better diastereoselectivity by comparing I2/Ph(OAc)2- with I2/Cu(OAc)2-mediated glycosylations using UV analysis have been conducted.
APA, Harvard, Vancouver, ISO, and other styles
16

Chen, Michael X., Ho-Hsuan Su, Ching-Ya Shiao, Yu-Ting Chang, Ming-Chu Chang, Chih-Chin Kao, San-Yuan Wang, Hsi-Chang Shih, and I.-Lin Tsai. "Affinity Purification Coupled to Stable Isotope Dilution LC-MS/MS Analysis to Discover IgG4 Glycosylation Profiles for Autoimmune Pancreatitis." International Journal of Molecular Sciences 22, no. 21 (October 26, 2021): 11527. http://dx.doi.org/10.3390/ijms222111527.

Full text
Abstract:
Type 1 autoimmune pancreatitis (AIP) is categorized as an IgG4-related disease (IgG4-RD), where a high concentration of plasma IgG4 is one of the common biomarkers among patients. IgG Fc-glycosylation has been reported to be potential biosignatures for diseases. However, human IgG3 and IgG4 Fc-glycopeptides from populations in Asia were found to be isobaric ions when using LC-MS/MS as an analytical tool. In this study, an analytical workflow that coupled affinity purification and stable isotope dilution LC-MS/MS was developed to dissect IgG4 glycosylation profiles for autoimmune pancreatitis. Comparing the IgG4 and glycosylation profiles among healthy controls, patients with pancreatic ductal adenocarcinoma (PDAC), and AIP, the IgG4 glycosylations from the AIP group were found to have more digalactosylation (compared to PDAC) and less monogalactosylation (compared to HC). In addition, higher fucosylation and sialylation profiles were also discovered for the AIP group. The workflow is efficient and selective for IgG4 glycopeptides, and can be used for clinical biosignature discovery.
APA, Harvard, Vancouver, ISO, and other styles
17

NISSEN, Nicholas N., Ravi SHANKAR, Richard L. GAMELLI, Ashok SINGH, and Luisa A. DiPIETRO. "Heparin and heparan sulphate protect basic fibroblast growth factor from non-enzymic glycosylation." Biochemical Journal 338, no. 3 (March 8, 1999): 637–42. http://dx.doi.org/10.1042/bj3380637.

Full text
Abstract:
Non-enzymic glycosylation of basic fibroblast growth factor (bFGF, FGF-2) has recently been demonstrated to decrease the mitogenic activity of intracellular bFGF. Loss of this bioactivity has been implicated in impaired wound healing and microangiopathies of diabetes mellitus. In addition to intracellular localization, bFGF is also widely distributed in the extracellular matrix, primarily bound to heparan sulphate proteoglycans (HSPGs). Nonetheless, it is not clear if non-enzymic glycosylation similarly inactivates matrix-bound bFGF. To investigate this, we measured the effect of non-enzymic glycosylation on bFGF bound to heparin, heparan sulphate and related compounds. Incubation of bFGF with the glycosylating agents glyceraldehyde 3-phosphate (G3P; 25 mM) or fructose (250 mM) resulted in loss of 90% and 40% of the mitogenic activity of bFGF respectively. Treatment with G3P and fructose also decreased the binding of bFGF to a heparin column. If heparin was added to bFGF prior to non-enzymic glycosylation, the mitogenic activity and heparin affinity of bFGF were nearly completely preserved. A similar protective effect was demonstrated by heparan sulphate, low-molecular-mass heparin and the polysaccharide dextran sulphate, but not by chondroitin sulphate. Whereas non-enzymic glycosylation of bFGF with G3P impaired its ability to stimulate c-myc mRNA expression in fibroblasts, no such impairment was noticeable when bFGF was glycosylated in the presence of heparin. Taken together, these results suggest that HSPG-bound bFGF is resistant to non-enzymic glycosylation-induced loss of activity. Therefore, alteration of this pool probably does not contribute to impaired wound healing seen in diabetes mellitus.
APA, Harvard, Vancouver, ISO, and other styles
18

Lahmann, Martina, and Stefan Oscarson. "Investigation of the reactivity difference between thioglycoside donors with variant aglycon parts." Canadian Journal of Chemistry 80, no. 8 (August 1, 2002): 889–93. http://dx.doi.org/10.1139/v02-101.

Full text
Abstract:
The reactivity of perbenzoylated thioglycosides with various thiol aglycons has been compared and quantified using competitive glycosylation experiments. Methyl 2,3,4-tri-O-benzyl-α-D-glucopyranoside was employed as acceptor and DMTST as a promoter. The reactivity was found, as expected, to depend on the electron donating properties of the aglycon. Hence, the most reactive donor, the cyclohexyl thioglycoside, was found to be about three times as reactive as the thioethyl glycoside, which in turn was twice as reactive as the thiomethyl donor. The thiophenyl donor was even less reactive, whereas p-halophenyl donors were inert under the glycosylation conditions used — but could be activated using NIS–TfOH as promoter. Furthermore, it was found that galactosyl donors were three to four times more reactive than the corresponding glucosyl derivative. These results allowed the design of an orthogonal coupling between thioglycosides with the same protecting groups (benzoyls) but with different thiol aglycons. Key words: thioglycosides, orthogonal glycosylations, competititive glycosylations.
APA, Harvard, Vancouver, ISO, and other styles
19

HART, G. "Glycosylation." Current Opinion in Cell Biology 4, no. 6 (December 1992): 1017–23. http://dx.doi.org/10.1016/0955-0674(92)90134-x.

Full text
APA, Harvard, Vancouver, ISO, and other styles
20

Warren, Charles E. "Glycosylation." Current Opinion in Biotechnology 4, no. 5 (October 1993): 596–602. http://dx.doi.org/10.1016/0958-1669(93)90083-9.

Full text
APA, Harvard, Vancouver, ISO, and other styles
21

Bandini, Giulia, Andreia Albuquerque-Wendt, Jan Hegermann, John Samuelson, and Françoise H. Routier. "Protein O- and C-Glycosylation pathways in Toxoplasma gondii and Plasmodium falciparum." Parasitology 146, no. 14 (February 18, 2019): 1755–66. http://dx.doi.org/10.1017/s0031182019000040.

Full text
Abstract:
AbstractApicomplexan parasites are amongst the most prevalent and morbidity-causing pathogens worldwide. They are responsible for severe diseases in humans and livestock and are thus of great public health and economic importance. Until the sequencing of apicomplexan genomes at the beginning of this century, the occurrence of N- and O-glycoproteins in these parasites was much debated. The synthesis of rudimentary and divergent N-glycans due to lineage-specific gene loss is now well established and has been recently reviewed. Here, we will focus on recent studies that clarified classical O-glycosylation pathways and described new nucleocytosolic glycosylations in Toxoplasma gondii, the causative agents of toxoplasmosis. We will also review the glycosylation of proteins containing thrombospondin type 1 repeats by O-fucosylation and C-mannosylation, newly discovered in Toxoplasma and the malaria parasite Plasmodium falciparum. The functional significance of these post-translational modifications has only started to emerge, but the evidence points towards roles for these protein glycosylation pathways in tissue cyst wall rigidity and persistence in the host, oxygen sensing, and stability of proteins involved in host invasion.
APA, Harvard, Vancouver, ISO, and other styles
22

Balieu, Juliette, Jae-Wan Jung, Philippe Chan, George P. Lomonossoff, Patrice Lerouge, and Muriel Bardor. "Investigation of the N-Glycosylation of the SARS-CoV-2 S Protein Contained in VLPs Produced in Nicotiana benthamiana." Molecules 27, no. 16 (August 11, 2022): 5119. http://dx.doi.org/10.3390/molecules27165119.

Full text
Abstract:
The emergence of the SARS-CoV-2 coronavirus pandemic in China in late 2019 led to the fast development of efficient therapeutics. Of the major structural proteins encoded by the SARS-CoV-2 genome, the SPIKE (S) protein has attracted considerable research interest because of the central role it plays in virus entry into host cells. Therefore, to date, most immunization strategies aim at inducing neutralizing antibodies against the surface viral S protein. The SARS-CoV-2 S protein is heavily glycosylated with 22 predicted N-glycosylation consensus sites as well as numerous mucin-type O-glycosylation sites. As a consequence, O- and N-glycosylations of this viral protein have received particular attention. Glycans N-linked to the S protein are mainly exposed at the surface and form a shield-masking specific epitope to escape the virus antigenic recognition. In this work, the N-glycosylation status of the S protein within virus-like particles (VLPs) produced in Nicotiana benthamiana (N. benthamiana) was investigated using a glycoproteomic approach. We show that 20 among the 22 predicted N-glycosylation sites are dominated by complex plant N-glycans and one carries oligomannoses. This suggests that the SARS-CoV-2 S protein produced in N. benthamiana adopts an overall 3D structure similar to that of recombinant homologues produced in mammalian cells.
APA, Harvard, Vancouver, ISO, and other styles
23

Ryu, Kyoung-Seok, Jie-Oh Lee, Taek Hun Kwon, Han-Ho Choi, Hong-Seog Park, Soo Kyung Hwang, Zee-Won Lee, et al. "The presence of monoglucosylated N196-glycan is important for the structural stability of storage protein, arylphorin." Biochemical Journal 421, no. 1 (June 12, 2009): 87–96. http://dx.doi.org/10.1042/bj20082170.

Full text
Abstract:
Although N-glycosylation has been known to increase the stability of glycoproteins, it is difficult to assess the structural importance of glycans in the stabilization of glycoproteins. APA (Antheraea pernyi arylphorin) is an insect hexamerin that has two N-glycosylations at Asn196 and Asn344 respectively. The glycosylation of Asn344 is critical for the folding process; however, glycosylation of Asn196 is not. Interestingly, the N196-glycan (glycosylation of Asn196) remains in an immature form (Glc1Man9GlcNAc2). The mutation of Asn196 to glutamine does not change the ecdysone-binding activity relative to that of the wild-type. In the present study, we determined the crystal structure of APA, and all sugar moieties of the N196-glycan were clearly observed in the electron-density map. Although the sugar moieties of the glycan generally have high structural flexibility, most sugar moieties of the N196-glycan were well organized in the deep cleft of the subunit interface and mediated many inter- and intrasubunit hydrogen bonds. Analytical ultracentrifugation and GdmCl (guanidinium chloride) unfolding experiments revealed that the presence of the N196-glycan was important for stabilizing the hexameric state and overall stability of APA respectively. Our results could provide a structural basis for studying not only other glycoproteins that carry an immature N-glycan, but also the structural role of N-glycans that are located in the deep cleft of a protein.
APA, Harvard, Vancouver, ISO, and other styles
24

O'Connell, B. C., and L. A. Tabak. "A Comparison of Serine and Threonine O-Glycosylation by UDP-GaINAc:Polypeptide N-Acetylgalactosaminyltransferase." Journal of Dental Research 72, no. 12 (December 1993): 1554–58. http://dx.doi.org/10.1177/00220345930720120401.

Full text
Abstract:
O-glycosylated proteins are ubiquitous in eukaryotes and are responsible for a variety of biological functions. O-glycosylation is initiated by the addition of N-acetylgalactosamine to serine or threonine residues, though it is not clear how specific residues are selected for modification. We have compared serine and threonine glycosylation using peptide substrates based on sequences from erythropoietin (EPO) and von Willebrand factor (HVF) that are glycosylated in vivo. UDP-GaINAc :polypeptide N-acetylgalactosaminyltransferase was derived from rat parotid, submandibular, and sublingual glands, liver and kidney as well as from human colostrum. The threonine-containing substrates were glycosylated to a much greater extent than those containing serine for all the enzyme sources. Changes in reaction pH, donor concentration, or divalent cation were unable to increase glycosylation of serine. When the incubation time was extended, serine in the EPObased peptide was found to incorporate GalNAc at a low level, in contrast to the serine-containing HVF peptide, which did not glycosylate at all. By circular dichroism, the non-glycosylating peptide was the only one of the series that did not exhibit random coil structure. Our data suggest that although the structural and sequence requirements for O-glycosylation of serine and threonine residues are similar, serine sites are glycosylated less effectively than are threonine sites in vitro.
APA, Harvard, Vancouver, ISO, and other styles
25

Downey, A. Michael, and Michal Hocek. "Strategies toward protecting group-free glycosylation through selective activation of the anomeric center." Beilstein Journal of Organic Chemistry 13 (June 27, 2017): 1239–79. http://dx.doi.org/10.3762/bjoc.13.123.

Full text
Abstract:
Glycosylation is an immensely important biological process and one that is highly controlled and very efficient in nature. However, in a chemical laboratory the process is much more challenging and usually requires the extensive use of protecting groups to squelch reactivity at undesired reactive moieties. Nonetheless, by taking advantage of the differential reactivity of the anomeric center, a selective activation at this position is possible. As a result, protecting group-free strategies to effect glycosylations are available thanks to the tremendous efforts of many research groups. In this review, we showcase the methods available for the selective activation of the anomeric center on the glycosyl donor and the mechanisms by which the glycosylation reactions take place to illustrate the power these techniques.
APA, Harvard, Vancouver, ISO, and other styles
26

Liang, Bing, Menglu Fan, Qi Meng, Yaping Zhang, Jiayu Jin, Na Chen, Yuanlu Lu, et al. "Effects of the Glycosylation of the HA Protein of H9N2 Subtype Avian Influenza Virus on the Pathogenicity in Mice and Antigenicity." Transboundary and Emerging Diseases 2024 (May 17, 2024): 1–18. http://dx.doi.org/10.1155/2024/6641285.

Full text
Abstract:
As the H9N2 subtype avian influenza virus (H9N2 AIV) evolves naturally, mutations in the hemagglutinin (HA) protein still occur, which involves some sites with glycosylations. It is widely established that glycosylation of the H9N2 AIV HA protein has a major impact on the antigenicity and pathogenicity of the virus. However, the biological implications of a particular glycosylation modification site (GMS) have not been well investigated. In this study, we generated viruses with different GMSs based on wild-type (WT) viruses. Antigenicity studies revealed that the presence of viruses with a 200G+/295G− mutation (with glycosylation at position 200 and deletion of glycosylation at position 295 in the HA protein) combined with a single GMS, such as 87G+, 127G+, 148G+, 178G+, or 265G+, could significantly affect the antigenicity of the virus. Pathogenicity assays revealed that the addition of GMS, such as 127G+, 188G+, 148G+, 178G+, or 54G+, decreased the virulence of the virus in mice, except for 87G+. The removal of GMS, such as 280G− or 295G−, increased the pathogenicity of the virus in mice. Further studies on pathogenicity revealed that 87G+/295G− could also enhance the pathogenicity of the virus. Finally, we selected the WT, WT-87G+, WT-295G−, and WT-87G+/295G− strains as our further research targets to investigate the detailed biological properties of the viruses. GMS, which can enhance viral pathogenicity, did not significantly affect replication or viral stability in vitro but significantly promoted the expression of proinflammatory factors to enhance inflammatory responses in mouse lungs. These findings further deepen our understanding of the influence of the glycosylation of the HA protein of H9N2 AIV on the pathogenicity and antigenicity of the virus in mice.
APA, Harvard, Vancouver, ISO, and other styles
27

Roy, Avishek, Steve Meregini, Zhenglan Chen, Evan Nair-Gill, Sara Ludwig, Jamie Russell, Jiexia Quan, et al. "IgE production and stability regulated by Glycosylation in vivo." Journal of Immunology 210, no. 1_Supplement (May 1, 2023): 151.19. http://dx.doi.org/10.4049/jimmunol.210.supp.151.19.

Full text
Abstract:
Abstract Rationale: Essential functions of IgE have been attributed to specific glycosylations such as oligomannose (Fcer1a binding) and sialylation (pathogenicity). However, no study has examined how glycosylation affects IgE stability in vivo. Methods: Forward genetic screening for IgE specific phenotypes was performed using N-ethyl-N-nitrosourea (ENU) mutagenized mice. One low IgE phenotype, named benadryl, linked to a mutation in Mpi, which is essential for N-linked glycosylation. Benadrylwas validated by CRISPR knock-in . Immunological studies were performed to determine the causative mechanism (passive/ active anaphylaxis, mast cell analysis, conditional knockout in T, B and dendritic cells, antibody production in vivoand in vitro, using IgE-Venus, IgE-KO, and IL-4 GFP mice). Results: Benadrylmice had low total and papain-specific IgE responses with resistance to active anaphylaxis. In vitroand in vivomast cell activation studies resulted in no difference in response to passive sensitization anaphylaxis. Both, in vivo and in vitro cellular staining in the conditional knockout showed no decrease in IgE B cells. IgE from Mpi deficient mice was produced and secreted from B cell culture. When de-glycosylated IgE was injected to IgE KO mice, it was cleared 10-fold faster than native IgE. Conclusions: Glycosylation status determines not only IgE functionality but in vivo stability. Mpi deficient mice produce IgE hypoglycosylated in nature and therefore it is cleared faster escaping anaphylaxis. Modulating IgE glycosylation represents a novel way to reduce IgE below pathogenic levels. NA
APA, Harvard, Vancouver, ISO, and other styles
28

Pasala, Chiranjeevi, Sahil Sharma, Tanaya Roychowdhury, Elisabetta Moroni, Giorgio Colombo, and Gabriela Chiosis. "N-Glycosylation as a Modulator of Protein Conformation and Assembly in Disease." Biomolecules 14, no. 3 (February 27, 2024): 282. http://dx.doi.org/10.3390/biom14030282.

Full text
Abstract:
Glycosylation, a prevalent post-translational modification, plays a pivotal role in regulating intricate cellular processes by covalently attaching glycans to macromolecules. Dysregulated glycosylation is linked to a spectrum of diseases, encompassing cancer, neurodegenerative disorders, congenital disorders, infections, and inflammation. This review delves into the intricate interplay between glycosylation and protein conformation, with a specific focus on the profound impact of N-glycans on the selection of distinct protein conformations characterized by distinct interactomes—namely, protein assemblies—under normal and pathological conditions across various diseases. We begin by examining the spike protein of the SARS virus, illustrating how N-glycans regulate the infectivity of pathogenic agents. Subsequently, we utilize the prion protein and the chaperone glucose-regulated protein 94 as examples, exploring instances where N-glycosylation transforms physiological protein structures into disease-associated forms. Unraveling these connections provides valuable insights into potential therapeutic avenues and a deeper comprehension of the molecular intricacies that underlie disease conditions. This exploration of glycosylation’s influence on protein conformation effectively bridges the gap between the glycome and disease, offering a comprehensive perspective on the therapeutic implications of targeting conformational mutants and their pathologic assemblies in various diseases. The goal is to unravel the nuances of these post-translational modifications, shedding light on how they contribute to the intricate interplay between protein conformation, assembly, and disease.
APA, Harvard, Vancouver, ISO, and other styles
29

Dobrica, Mihaela-Olivia, Catalin Lazar, and Norica Branza-Nichita. "N-Glycosylation and N-Glycan Processing in HBV Biology and Pathogenesis." Cells 9, no. 6 (June 4, 2020): 1404. http://dx.doi.org/10.3390/cells9061404.

Full text
Abstract:
Hepatitis B Virus (HBV) glycobiology has been an area of intensive research in the last decades and continues to be an attractive topic due to the multiple roles that N-glycosylation in particular plays in the virus life-cycle and its interaction with the host that are still being discovered. The three HBV envelope glycoproteins, small (S), medium (M) and large (L) share a very peculiar N-glycosylation pattern, which distinctly regulates their folding, degradation, assembly, intracellular trafficking and antigenic properties. In addition, recent findings indicate important roles of N-linked oligosaccharides in viral pathogenesis and evasion of the immune system surveillance. This review focuses on N-glycosylation’s contribution to HBV infection and disease, with implications for development of improved vaccines and antiviral therapies.
APA, Harvard, Vancouver, ISO, and other styles
30

Whitfield, Dennis M., M. Younus Meah, and Jiří J. Křepinský. "Ultrasonic Agitation Accelerates cis-Glycosylation with Heterogeneous Promoters." Collection of Czechoslovak Chemical Communications 58, no. 1 (1993): 159–72. http://dx.doi.org/10.1135/cccc19930159.

Full text
Abstract:
Ultrasonic agitation increases the yield of glycosylations with donors such as 3,4,6-tri-O-acetyl-2-azido-2-deoxy-α-D-galactopyranosyl chloride using the heterogeneous promoters silver zeolite, cadmium zeolite or a mixture of silver perchlorate and silver carbonate on celite. The stereospecificity of the glycosylation depends on the nature of the alcohol to be glycosylated, the nature of the solid support and the solvent. Glycosylation catalyzed by silver zeolite in toluene solutions of the donor 3,4,6-tri-O-acetyl-2-deoxy-2-phtalimido-β-D-glucopyranosyl bromide, that usually produce trans-β-glycosides, yield cis-glycosides with unreactive alcohols. In these unreactive alcohols, e.g. methyl 2-O-benzoyl-4,6-O-benzilidene-β-D-galactopyranoside and benzyl 3,4,6-tri-O-benzyl-α-D-mannopyranoside, the hydroxyls to be glycosylated are hydrogen-bonded to a cis vicinal oxygen. This feature was evident in their AM1 minimized conformations and was indicated by the solution J(OH,CH) 1H NMR coupling constants.
APA, Harvard, Vancouver, ISO, and other styles
31

Sasaki, Kaname, and Yusuke Hashimoto. "2,6-Lactones as a New Entry in Stereoselective Glycosylations." Synlett 28, no. 10 (February 23, 2017): 1121–26. http://dx.doi.org/10.1055/s-0036-1588722.

Full text
Abstract:
The advantages of glycosyl donors bearing a 2,6-lactone moiety in 1,2-cis-β-glycosylation reactions are discussed in the context of recent comprehension on the SN2–SN1 borderline. The 2,6-lactone structure increases the likelihood of the SN2-like reaction, analogous to 4,6-tethered structures or 2-O-electron-deficient substituents, which are known to mound the energetic barrier to SN1 reactions. Furthermore, the glycosyl cation generated from the 2,6-lactone donor seems to direct β-glycosides similar to the torsional and flipped cations generated from 4,6-tethered donors and mannuronate or 3,6-lactone donors, respectively. Overall, 2,6-lactones are suitable for use in 1,2-cis-β-glycosylations, and this novel class of donors is expected to help deepen our global understanding of glycosylation reactions.1 Introduction2 Stereoinversion (SN2-Like) Reactions3 Conformational Control of Glycosyl Cations4 Conclusions
APA, Harvard, Vancouver, ISO, and other styles
32

Masbuchin, Ainun Nizar, Mohammad Saifur Rohman, and Ping-Yen Liu. "Role of Glycosylation in Vascular Calcification." International Journal of Molecular Sciences 22, no. 18 (September 11, 2021): 9829. http://dx.doi.org/10.3390/ijms22189829.

Full text
Abstract:
Glycosylation is an important step in post-translational protein modification. Altered glycosylation results in an abnormality that causes diseases such as malignancy and cardiovascular diseases. Recent emerging evidence highlights the importance of glycosylation in vascular calcification. Two major types of glycosylation, N-glycosylation and O-glycosylation, are involved in vascular calcification. Other glycosylation mechanisms, which polymerize the glycosaminoglycan (GAG) chain onto protein, resulting in proteoglycan (PG), also have an impact on vascular calcification. This paper discusses the role of glycosylation in vascular calcification.
APA, Harvard, Vancouver, ISO, and other styles
33

Jia, Xiao G., and Alexei V. Demchenko. "Intramolecular glycosylation." Beilstein Journal of Organic Chemistry 13 (September 29, 2017): 2028–48. http://dx.doi.org/10.3762/bjoc.13.201.

Full text
Abstract:
Carbohydrate oligomers remain challenging targets for chemists due to the requirement for elaborate protecting and leaving group manipulations, functionalization, tedious purification, and sophisticated characterization. Achieving high stereocontrol in glycosylation reactions is arguably the major hurdle that chemists experience. This review article overviews methods for intramolecular glycosylation reactions wherein the facial stereoselectivity is achieved by tethering of the glycosyl donor and acceptor counterparts.
APA, Harvard, Vancouver, ISO, and other styles
34

Ernst, J. F., and S. K. H. Prill. "O-Glycosylation." Medical Mycology 39, no. 1 (January 2001): 67–74. http://dx.doi.org/10.1080/mmy.39.1.67.74.

Full text
APA, Harvard, Vancouver, ISO, and other styles
35

Stanley, P. "Golgi Glycosylation." Cold Spring Harbor Perspectives in Biology 3, no. 4 (March 2, 2011): a005199. http://dx.doi.org/10.1101/cshperspect.a005199.

Full text
APA, Harvard, Vancouver, ISO, and other styles
36

Stanley, Pamela. "Glycosylation engineering." Glycobiology 2, no. 2 (1992): 99–107. http://dx.doi.org/10.1093/glycob/2.2.99.

Full text
APA, Harvard, Vancouver, ISO, and other styles
37

Williams, Ruth. "Glycosylation PERKs." Journal of Cell Biology 176, no. 5 (February 26, 2007): 549b. http://dx.doi.org/10.1083/jcb.1765iti4.

Full text
APA, Harvard, Vancouver, ISO, and other styles
38

Ernst, J. F., and S. K. H. Prill. "O -Glycosylation." Medical Mycology 39, no. 1 (December 15, 2001): 67–74. http://dx.doi.org/10.1080/744118884.

Full text
APA, Harvard, Vancouver, ISO, and other styles
39

Wang, Hongda, Linda Obenauer-Kutner, Mei Lin, Yunping Huang, Michael J. Grace, and Stuart M. Lindsay. "Imaging Glycosylation." Journal of the American Chemical Society 130, no. 26 (July 2008): 8154–55. http://dx.doi.org/10.1021/ja802535p.

Full text
APA, Harvard, Vancouver, ISO, and other styles
40

Křen, Vladimír, Petr Halada, and Petr Sedmera. "Agroclavine Glycosylation." Collection of Czechoslovak Chemical Communications 64, no. 1 (1999): 114–18. http://dx.doi.org/10.1135/cccc19990114.

Full text
APA, Harvard, Vancouver, ISO, and other styles
41

BORMAN, STU. "GLYCOSYLATION ENGINEERING." Chemical & Engineering News Archive 84, no. 36 (September 4, 2006): 13–22. http://dx.doi.org/10.1021/cen-v084n036.p013.

Full text
APA, Harvard, Vancouver, ISO, and other styles
42

Parslow, G. P., and E. J. Wood. "Protein glycosylation." Biochemical Education 26, no. 2 (April 1998): 145. http://dx.doi.org/10.1016/s0307-4412(98)00126-5.

Full text
APA, Harvard, Vancouver, ISO, and other styles
43

Kennedy, John F., and Charles J. Knill. "Protein Glycosylation." Carbohydrate Polymers 46, no. 4 (December 2001): 393. http://dx.doi.org/10.1016/s0144-8617(01)00251-x.

Full text
APA, Harvard, Vancouver, ISO, and other styles
44

Hennet, Thierry. "Collagen glycosylation." Current Opinion in Structural Biology 56 (June 2019): 131–38. http://dx.doi.org/10.1016/j.sbi.2019.01.015.

Full text
APA, Harvard, Vancouver, ISO, and other styles
45

Ploegh, H., and J. J. Neefjes. "Protein glycosylation." Current Opinion in Cell Biology 2, no. 6 (December 1990): 1125–30. http://dx.doi.org/10.1016/0955-0674(90)90166-c.

Full text
APA, Harvard, Vancouver, ISO, and other styles
46

Delente, Jacques J. "Glycosylation revisited." Trends in Biotechnology 3, no. 9 (September 1985): 218. http://dx.doi.org/10.1016/0167-7799(85)90009-5.

Full text
APA, Harvard, Vancouver, ISO, and other styles
47

März, Leopold. "Glycosylation reconfirmed." Trends in Biotechnology 4, no. 4 (April 1986): 81. http://dx.doi.org/10.1016/0167-7799(86)90199-x.

Full text
APA, Harvard, Vancouver, ISO, and other styles
48

West, Christopher M. "Nucleocytoplasmic Glycosylation." Biochimica et Biophysica Acta (BBA) - General Subjects 1800, no. 2 (February 2010): 47–48. http://dx.doi.org/10.1016/j.bbagen.2009.12.008.

Full text
APA, Harvard, Vancouver, ISO, and other styles
49

Singh, Yashapal, Tinghua Wang, Scott A. Geringer, Keith J. Stine, and Alexei V. Demchenko. "Regenerative Glycosylation." Journal of Organic Chemistry 83, no. 1 (December 22, 2017): 374–81. http://dx.doi.org/10.1021/acs.joc.7b02768.

Full text
APA, Harvard, Vancouver, ISO, and other styles
50

Ernst, J. F., and S. K. H. Prill. "O-Glycosylation." Medical Mycology 39, no. 1 (December 15, 2001): 67–74. http://dx.doi.org/10.1080/714031008.

Full text
APA, Harvard, Vancouver, ISO, and other styles
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography